ID D0KMU6_SULS9 Unreviewed; 249 AA. AC D0KMU6; DT 15-DEC-2009, integrated into UniProtKB/TrEMBL. DT 15-DEC-2009, sequence version 1. DT 07-NOV-2018, entry version 49. DE RecName: Full=NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000256|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000256|HAMAP-Rule:MF_00361}; GN Name=nadK {ECO:0000256|HAMAP-Rule:MF_00361}; GN OrderedLocusNames=Ssol_0037 {ECO:0000313|EMBL:ACX90342.1}; OS Sulfolobus solfataricus (strain 98/2). OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=555311 {ECO:0000313|EMBL:ACX90342.1, ECO:0000313|Proteomes:UP000001493}; RN [1] {ECO:0000313|EMBL:ACX90342.1, ECO:0000313|Proteomes:UP000001493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=98/2 {ECO:0000313|EMBL:ACX90342.1, RC ECO:0000313|Proteomes:UP000001493}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., RA Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., RA Ovchinnikova G., Mead D.; RT "Complete sequence of Sulfolobus solfataricus 98/2."; RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. CC Catalyzes specifically the phosphorylation on 2'-hydroxyl of the CC adenosine moiety of NAD to yield NADP. {ECO:0000256|HAMAP- CC Rule:MF_00361}. CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). CC {ECO:0000256|HAMAP-Rule:MF_00361}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00361}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}. CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000256|HAMAP- CC Rule:MF_00361}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00361}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001800; ACX90342.1; -; Genomic_DNA. DR RefSeq; WP_009992063.1; NZ_ACUK01000288.1. DR ProteinModelPortal; D0KMU6; -. DR SMR; D0KMU6; -. DR EnsemblBacteria; ACX90342; ACX90342; Ssol_0037. DR GeneID; 27428541; -. DR KEGG; sol:Ssol_0037; -. DR HOGENOM; HOG000270621; -. DR KO; K00858; -. DR OMA; VNLGHVG; -. DR OrthoDB; POG093Z0ENK; -. DR Proteomes; UP000001493; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003951; F:NAD+ kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IEA:UniProtKB-UniRule. DR Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 1. DR HAMAP; MF_00361; NAD_kinase; 1. DR InterPro; IPR017438; ATP-NAD_kinase_N. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C. DR InterPro; IPR016064; NAD/diacylglycerol_kinase_sf. DR InterPro; IPR002504; NADK. DR Pfam; PF01513; NAD_kinase; 1. DR SUPFAM; SSF111331; SSF111331; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00361}; KW Complete proteome {ECO:0000313|Proteomes:UP000001493}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00361}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00361, ECO:0000313|EMBL:ACX90342.1}; KW NAD {ECO:0000256|HAMAP-Rule:MF_00361}; KW NADP {ECO:0000256|HAMAP-Rule:MF_00361}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00361}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00361, KW ECO:0000313|EMBL:ACX90342.1}. FT NP_BIND 45 46 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT NP_BIND 110 111 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT NP_BIND 149 154 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT ACT_SITE 45 45 Proton acceptor. {ECO:0000256|HAMAP-Rule: FT MF_00361}. FT BINDING 50 50 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. FT BINDING 138 138 NAD. {ECO:0000256|HAMAP-Rule:MF_00361}. SQ SEQUENCE 249 AA; 27890 MW; D4AD6A9F7DCD8A49 CRC64; MRVKIVSKPT SQLNYTVEKI KNISNKLGFE VVDIDFDYVI AVGGDGTLLR AVKLGKPVIA IKAGRRGLLM DVPVDKIEDA LLRLKKGDYN EEEYMLLEMV HNDKVELGFN EIGILYDRPE AIKVGISFDT ERVSVEGDGV LVSTPQGSSG WGMSATNSLL YKDLNAIEII FVNPIFYYLR SVVIPPKSLI LRLEDKGYPQ TARVVVDGEV VTLIKTNQEI TVRVSQHKAK ILRFFKLDLI GEVLHAYHI //